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SH3L3_MOUSE
ID   SH3L3_MOUSE             Reviewed;          93 AA.
AC   Q91VW3;
DT   01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 152.
DE   RecName: Full=SH3 domain-binding glutamic acid-rich-like protein 3;
GN   Name=Sh3bgrl3;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11444877; DOI=10.1006/bbrc.2001.5169;
RA   Mazzocco M., Arrigo P., Egeo A., Maffei M., Vergano A., Di Lisi R.,
RA   Ghiotto F., Ciccone E., Cinti R., Ravazzolo R., Scartezzini P.;
RT   "A novel human homologue of the SH3BGR gene encodes a small protein similar
RT   to glutaredoxin 1 of Escherichia coli.";
RL   Biochem. Biophys. Res. Commun. 285:540-545(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PROTEIN SEQUENCE OF 6-15; 285-302 AND 562-572, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RA   Lubec G., Kang S.U.;
RL   Submitted (APR-2007) to UniProtKB.
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND SUBUNIT.
RX   PubMed=15120624; DOI=10.1016/j.bbrc.2004.04.050;
RA   Nardini M., Mazzocco M., Massaro A., Maffei M., Vergano A., Donadini A.,
RA   Scartezzini P., Bolognesi M.;
RT   "Crystal structure of the glutaredoxin-like protein SH3BGRL3 at 1.6
RT   Angstrom resolution.";
RL   Biochem. Biophys. Res. Commun. 318:470-476(2004).
RN   [7]
RP   STRUCTURE BY NMR.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of the SH3 domain binding glutamic acid-rich protein
RT   like 3.";
RL   Submitted (DEC-2003) to the PDB data bank.
CC   -!- FUNCTION: Could act as a modulator of glutaredoxin biological activity.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15120624}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SH3BGR family. {ECO:0000305}.
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DR   EMBL; AK003431; BAC25034.1; -; mRNA.
DR   EMBL; BC008110; AAH08110.1; -; mRNA.
DR   CCDS; CCDS38910.1; -.
DR   RefSeq; NP_542126.1; NM_080559.1.
DR   PDB; 1J0F; NMR; -; A=1-93.
DR   PDB; 1T1V; X-ray; 1.60 A; A/B=1-93.
DR   PDBsum; 1J0F; -.
DR   PDBsum; 1T1V; -.
DR   AlphaFoldDB; Q91VW3; -.
DR   BMRB; Q91VW3; -.
DR   SMR; Q91VW3; -.
DR   BioGRID; 216213; 1.
DR   IntAct; Q91VW3; 1.
DR   STRING; 10090.ENSMUSP00000030651; -.
DR   iPTMnet; Q91VW3; -.
DR   PhosphoSitePlus; Q91VW3; -.
DR   SwissPalm; Q91VW3; -.
DR   CPTAC; non-CPTAC-4007; -.
DR   EPD; Q91VW3; -.
DR   jPOST; Q91VW3; -.
DR   MaxQB; Q91VW3; -.
DR   PaxDb; Q91VW3; -.
DR   PeptideAtlas; Q91VW3; -.
DR   PRIDE; Q91VW3; -.
DR   ProteomicsDB; 257141; -.
DR   Antibodypedia; 30595; 145 antibodies from 25 providers.
DR   Ensembl; ENSMUST00000030651; ENSMUSP00000030651; ENSMUSG00000028843.
DR   GeneID; 73723; -.
DR   KEGG; mmu:73723; -.
DR   UCSC; uc008vec.1; mouse.
DR   CTD; 83442; -.
DR   MGI; MGI:1920973; Sh3bgrl3.
DR   VEuPathDB; HostDB:ENSMUSG00000028843; -.
DR   eggNOG; KOG4023; Eukaryota.
DR   GeneTree; ENSGT00940000157260; -.
DR   HOGENOM; CLU_084862_3_1_1; -.
DR   InParanoid; Q91VW3; -.
DR   OMA; FFNEDQY; -.
DR   OrthoDB; 1508713at2759; -.
DR   PhylomeDB; Q91VW3; -.
DR   TreeFam; TF105574; -.
DR   BioGRID-ORCS; 73723; 3 hits in 73 CRISPR screens.
DR   ChiTaRS; Sh3bgrl3; mouse.
DR   EvolutionaryTrace; Q91VW3; -.
DR   PRO; PR:Q91VW3; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q91VW3; protein.
DR   Bgee; ENSMUSG00000028843; Expressed in peripheral lymph node and 260 other tissues.
DR   ExpressionAtlas; Q91VW3; baseline and differential.
DR   Genevisible; Q91VW3; MM.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016604; C:nuclear body; ISO:MGI.
DR   CDD; cd03030; GRX_SH3BGR; 1.
DR   InterPro; IPR006993; Glut_rich_SH3-bd.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF04908; SH3BGR; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS51354; GLUTAREDOXIN_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; Nucleus;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H299"
FT   CHAIN           2..93
FT                   /note="SH3 domain-binding glutamic acid-rich-like protein
FT                   3"
FT                   /id="PRO_0000220750"
FT   DOMAIN          2..93
FT                   /note="Glutaredoxin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00686"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H299"
FT   STRAND          4..8
FT                   /evidence="ECO:0007829|PDB:1T1V"
FT   HELIX           15..30
FT                   /evidence="ECO:0007829|PDB:1T1V"
FT   STRAND          36..39
FT                   /evidence="ECO:0007829|PDB:1T1V"
FT   TURN            40..42
FT                   /evidence="ECO:0007829|PDB:1J0F"
FT   HELIX           44..53
FT                   /evidence="ECO:0007829|PDB:1T1V"
FT   STRAND          63..66
FT                   /evidence="ECO:0007829|PDB:1T1V"
FT   STRAND          69..73
FT                   /evidence="ECO:0007829|PDB:1T1V"
FT   HELIX           74..82
FT                   /evidence="ECO:0007829|PDB:1T1V"
FT   HELIX           86..89
FT                   /evidence="ECO:0007829|PDB:1T1V"
SQ   SEQUENCE   93 AA;  10477 MW;  DB89688F0C5B82CC CRC64;
     MSGLRVYSTS VTGSREIKSQ QSEVTRILDG KRIQYQLVDI SQDNALRDEM RTLAGNPKAT
     PPQIVNGNHY CGDYELFVEA VEQDTLQEFL KLA
 
 
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